EFTS_COPPD
ID EFTS_COPPD Reviewed; 197 AA.
AC B5Y8J0;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 25-MAY-2022, entry version 69.
DE RecName: Full=Elongation factor Ts {ECO:0000255|HAMAP-Rule:MF_00050};
DE Short=EF-Ts {ECO:0000255|HAMAP-Rule:MF_00050};
GN Name=tsf {ECO:0000255|HAMAP-Rule:MF_00050};
GN OrderedLocusNames=COPRO5265_0739;
OS Coprothermobacter proteolyticus (strain ATCC 35245 / DSM 5265 / OCM 4 /
OS BT).
OC Bacteria; Coprothermobacterota; Coprothermobacteria; Coprothermobacterales;
OC Coprothermobacteraceae; Coprothermobacter.
OX NCBI_TaxID=309798;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35245 / DSM 5265 / OCM 4 / BT;
RA Dodson R.J., Durkin A.S., Wu M., Eisen J., Sutton G.;
RT "The complete genome sequence of Coprothermobacter proteolyticus strain
RT ATCC 5245 / DSM 5265 / BT.";
RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Associates with the EF-Tu.GDP complex and induces the
CC exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-
CC Tu.GTP complex up to the GTP hydrolysis stage on the ribosome.
CC {ECO:0000255|HAMAP-Rule:MF_00050}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00050}.
CC -!- SIMILARITY: Belongs to the EF-Ts family. {ECO:0000255|HAMAP-
CC Rule:MF_00050}.
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DR EMBL; CP001145; ACI17943.1; -; Genomic_DNA.
DR RefSeq; WP_012544594.1; NC_011295.1.
DR AlphaFoldDB; B5Y8J0; -.
DR SMR; B5Y8J0; -.
DR STRING; 309798.COPRO5265_0739; -.
DR EnsemblBacteria; ACI17943; ACI17943; COPRO5265_0739.
DR KEGG; cpo:COPRO5265_0739; -.
DR eggNOG; COG0264; Bacteria.
DR HOGENOM; CLU_047155_1_1_9; -.
DR OMA; DAGMMDC; -.
DR OrthoDB; 1405357at2; -.
DR Proteomes; UP000001732; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.479.20; -; 1.
DR HAMAP; MF_00050; EF_Ts; 1.
DR InterPro; IPR036402; EF-Ts_dimer_sf.
DR InterPro; IPR001816; Transl_elong_EFTs/EF1B.
DR InterPro; IPR014039; Transl_elong_EFTs/EF1B_dimer.
DR InterPro; IPR018101; Transl_elong_Ts_CS.
DR InterPro; IPR009060; UBA-like_sf.
DR PANTHER; PTHR11741; PTHR11741; 1.
DR Pfam; PF00889; EF_TS; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR SUPFAM; SSF54713; SSF54713; 1.
DR TIGRFAMs; TIGR00116; tsf; 1.
DR PROSITE; PS01126; EF_TS_1; 1.
DR PROSITE; PS01127; EF_TS_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Elongation factor; Protein biosynthesis; Reference proteome.
FT CHAIN 1..197
FT /note="Elongation factor Ts"
FT /id="PRO_1000189871"
FT REGION 81..84
FT /note="Involved in Mg(2+) ion dislocation from EF-Tu"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00050"
SQ SEQUENCE 197 AA; 22140 MW; 8CBD2C0F8DBF4E11 CRC64;
MEISASLVKQ LRDETGAGFM ECKKALEETG GDLEKAKLVL KEKGLARAEK KIGRAASQGL
IHAYIHGEGK LGVLVEVNCE TDFVARTDDF KELVHEIALQ IAGMAPEYVA VEDVPEEVIE
QEKEIYRKQA ENEGKPAEII DKIVEGKLQN FYKSKVLLEQ PYVRDDSKTI KDLIKEKIAL
LGENIVVRRF VRWTLGE